메뉴 건너뛰기




Volumn 287, Issue 10, 2012, Pages 7456-7466

Structural model of channelrhodopsin

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; ATOMIC LEVELS; CATION CHANNELS; COMPUTATIONAL APPROACH; DUNALIELLA SALINA; FUNCTIONAL MECHANISMS; ION TRANSPORTS; LIVING ANIMALS; MICRO-ALGAE; MODEL-BASED OPC; STRUCTURAL MODELS; STRUCTURAL MOTIFS;

EID: 84863229159     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.320309     Document Type: Article
Times cited : (36)

References (50)
  • 1
    • 0037189362 scopus 로고    scopus 로고
    • Channelrhodopsin-1: A light-gated proton channel in green algae
    • DOI 10.1126/science.1072068
    • Nagel, G., Ollig, D., Fuhrmann, M., Kateriya, S., Musti, A. M., Bamberg, E., and Hegemann, P. (2002) Channelrhodopsin-1. A light-gated proton channel in green algae. Science 296, 2395-2398 (Pubitemid 34734214)
    • (2002) Science , vol.296 , Issue.5577 , pp. 2395-2398
    • Nagel, G.1    Ollig, D.2    Fuhrmann, M.3    Kateriya, S.4    Musti, A.M.5    Bamberg, E.6    Hegemann, P.7
  • 5
    • 26444621497 scopus 로고    scopus 로고
    • Millisecond-timescale, genetically targeted optical control of neural activity
    • DOI 10.1038/nn1525, PII N1525
    • Boyden, E. S., Zhang, F., Bamberg, E., Nagel, G., and Deisseroth, K. (2005) Millisecond-timescale, genetically targeted optical control of neural activity. Nat. Neurosci. 8, 1263-1268 (Pubitemid 43348147)
    • (2005) Nature Neuroscience , vol.8 , Issue.9 , pp. 1263-1268
    • Boyden, E.S.1    Zhang, F.2    Bamberg, E.3    Nagel, G.4    Deisseroth, K.5
  • 6
    • 30944451943 scopus 로고    scopus 로고
    • Kinetic evaluation of photosensitivity in genetically engineered neurons expressing green algae light-gated channels
    • DOI 10.1016/j.neures.2005.10.009, PII S0168010205002762
    • Ishizuka, T., Kakuda, M., Araki, R., and Yawo, H. (2006) Kinetic evaluation of photosensitivity in genetically engineered neurons expressing green algae light-gated channels. Neurosci. Res. 54, 85-94 (Pubitemid 43112092)
    • (2006) Neuroscience Research , vol.54 , Issue.2 , pp. 85-94
    • Ishizuka, T.1    Kakuda, M.2    Araki, R.3    Yawo, H.4
  • 8
    • 36248996490 scopus 로고    scopus 로고
    • Neural substrates of awakening probed with optogenetic control of hypocretin neurons
    • DOI 10.1038/nature06310, PII NATURE06310
    • Adamantidis, A. R., Zhang, F., Aravanis, A. M., Deisseroth, K., and de Lecea, L. (2007) Neural substrates of awakening probed with optogenetic control of hypocretin neurons. Nature 450, 420-424 (Pubitemid 350126754)
    • (2007) Nature , vol.450 , Issue.7168 , pp. 420-424
    • Adamantidis, A.R.1    Zhang, F.2    Aravanis, A.M.3    Deisseroth, K.4    De Lecea, L.5
  • 9
    • 79959873914 scopus 로고    scopus 로고
    • The development and application of optogenetics
    • Fenno, L., Yizhar, O., and Deisseroth, K. (2011) The development and application of optogenetics. Annu. Rev. Neurosci. 34, 389-412
    • (2011) Annu. Rev. Neurosci. , vol.34 , pp. 389-412
    • Fenno, L.1    Yizhar, O.2    Deisseroth, K.3
  • 10
    • 81055155876 scopus 로고    scopus 로고
    • Projection structure of channelrhodopsin-2 at 6 Å resolution by electron crystallography
    • Müller, M., Bamann, C., Bamberg, E., and Kühlbrandt, W. (2011) Projection structure of channelrhodopsin-2 at 6 Å resolution by electron crystallography. J. Mol. Biol. 414, 86-95
    • (2011) J. Mol. Biol. , vol.414 , pp. 86-95
    • Müller, M.1    Bamann, C.2    Bamberg, E.3    Kühlbrandt, W.4
  • 11
    • 0035999985 scopus 로고    scopus 로고
    • Amphiphilicity index index of polar amino acids as an aid in the characterization of amino acid preference at membrane-water interfaces
    • Mitaku, S., Hirokawa, T., and Tsuji, T. (2002) Amphiphilicity index of polar amino acids as an aid in the characterization of amino acid preference at membrane-water interfaces. Bioinformatics 18, 608-616 (Pubitemid 34521049)
    • (2002) Bioinformatics , vol.18 , Issue.4 , pp. 608-616
    • Mitaku, S.1    Hirokawa, T.2    Tsuji, T.3
  • 12
    • 53349103176 scopus 로고    scopus 로고
    • Simulations of a G protein-coupled receptor homology model predict dynamic features and a ligand binding site
    • Wolf, S., Böckmann, M., Höweler, U., Schlitter, J., and Gerwert, K. (2008) Simulations of a G protein-coupled receptor homology model predict dynamic features and a ligand binding site. FEBS Lett. 582, 3335-3342
    • (2008) FEBS Lett. , vol.582 , pp. 3335-3342
    • Wolf, S.1    Böckmann, M.2    Höweler, U.3    Schlitter, J.4    Gerwert, K.5
  • 13
    • 78650826238 scopus 로고    scopus 로고
    • Molecular mechanism of long-range synergetic color tuning between multiple amino acid residues in conger rhodopsin
    • Watanabe, H. C., Mori, Y., Tada, T., Yokoyama, S., and Yamato, T. (2010) Molecular mechanism of long-range synergetic color tuning between multiple amino acid residues in conger rhodopsin. Biophysics 6, 67-68
    • (2010) Biophysics , vol.6 , pp. 67-68
    • Watanabe, H.C.1    Mori, Y.2    Tada, T.3    Yokoyama, S.4    Yamato, T.5
  • 15
    • 8844250818 scopus 로고    scopus 로고
    • Anabaena sensory rhodopsin: A photochromic color sensor at 2.0 A
    • DOI 10.1126/science.1103943
    • Vogeley, L., Sineshchekov, O. A., Trivedi, V. D., Sasaki, J., Spudich, J. L., and Luecke, H. (2004) Anabaena sensory rhodopsin. A photochromic color sensor at 2.0 A. Science 306, 1390-1393 (Pubitemid 39532519)
    • (2004) Science , vol.306 , Issue.5700 , pp. 1390-1393
    • Vogeley, L.1    Sineshchekov, O.A.2    Trivedi, V.D.3    Sasaki, J.4    Spudich, J.L.5    Luecke, H.6
  • 16
    • 11844302809 scopus 로고    scopus 로고
    • Energetics of quinone-dependent electron and proton transfers in Rhodobacter sphaeroides photosynthetic reaction centers
    • DOI 10.1021/bi048348k
    • Zhu, Z., and Gunner, M. R. (2005) Energetics of quinone-dependent electron and proton transfers in Rhodobacter sphaeroides photosynthetic reaction centers. Biochemistry 44, 82-96 (Pubitemid 40095709)
    • (2005) Biochemistry , vol.44 , Issue.1 , pp. 82-96
    • Zhu, Z.1    Gunner, M.R.2
  • 17
    • 79951476387 scopus 로고    scopus 로고
    • PROPKA3: Consistent treatment of internal and surface residues in empirical pK(a) predictions
    • Olsson, M. H. M., Sondergaard, C. R., Rostkowski, M., and Jensen, J. H. (2011) PROPKA3: Consistent treatment of internal and surface residues in empirical pK(a) predictions. J. Chem. Theory Comput. 7, 525-537
    • (2011) J. Chem. Theory Comput. , vol.7 , pp. 525-537
    • Olsson, M.H.M.1    Sondergaard, C.R.2    Rostkowski, M.3    Jensen, J.H.4
  • 19
    • 0037116518 scopus 로고    scopus 로고
    • Polyunsaturated fatty acids in lipid bilayers: Intrinsic and environmental contributions to their unique physical properties
    • DOI 10.1021/ja0118340
    • Feller, S. E., Gawrisch, K., and MacKerell, A. D. (2002) Polyunsaturated fatty acids in lipid bilayers. Intrinsic and environmental contributions to their unique physical properties. J. Am. Chem. Soc. 124, 318-326 (Pubitemid 34062762)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.2 , pp. 318-326
    • Feller, S.E.1    Gawrisch, K.2    MacKerell Jr., A.D.3
  • 22
    • 0038056334 scopus 로고    scopus 로고
    • A charge-scaling method to treat solvent in QM/MM simulations
    • DOI 10.1007/s00214-002-0417-z
    • Dinner, A. R., Lopez, X., and Karplus, M. (2003) A charge-scaling method to treat solvent in QM/MM simulations. Theor. Chem. Acc. 109, 118-124 (Pubitemid 36589176)
    • (2003) Theoretical Chemistry Accounts , vol.109 , Issue.3 , pp. 118-124
    • Dinner, A.R.1    Lopez, X.2    Karplus, M.3
  • 23
    • 0344667545 scopus 로고    scopus 로고
    • A spectroscopy oriented configuration interaction procedure
    • Neese, F. (2003) A spectroscopy oriented configuration interaction procedure. J. Chem. Phys. 119, 9428-9443
    • (2003) J. Chem. Phys. , vol.119 , pp. 9428-9443
    • Neese, F.1
  • 25
    • 57349151754 scopus 로고    scopus 로고
    • Channelrhodopsin-1 initiates phototaxis and photophobic responses in Chlamydomonas by immediate light-induced depolarization
    • DOI 10.1105/tpc.108.057919
    • Berthold, P., Tsunoda, S. P., Ernst, O. P., Mages, W., Gradmann, D., and Hegemann, P. (2008) Channelrhodopsin-1 initiates phototaxis and photophobic responses in Chlamydomonas by immediate light-induced depolarization. Plant Cell 20, 1665-1677 (Pubitemid 352844170)
    • (2008) Plant Cell , vol.20 , Issue.6 , pp. 1665-1677
    • Berthold, P.1    Tsunoda, S.P.2    Ernst, O.P.3    Mages, W.4    Gradmann, D.5    Hegemanna, P.6
  • 27
    • 79960338849 scopus 로고    scopus 로고
    • Glutamate residue 90 in the predicted transmembrane domain 2 is crucial for cation flux through channelrhodopsin 2
    • Ruffert, K., Himmel, B., Lall, D., Bamann, C., Bamberg, E., Betz, H., and Eulenburg, V. (2011) Glutamate residue 90 in the predicted transmembrane domain 2 is crucial for cation flux through channelrhodopsin 2. Biochem. Biophys. Res. Commun. 410, 737-743
    • (2011) Biochem. Biophys. Res. Commun. , vol.410 , pp. 737-743
    • Ruffert, K.1    Himmel, B.2    Lall, D.3    Bamann, C.4    Bamberg, E.5    Betz, H.6    Eulenburg, V.7
  • 28
    • 84855190225 scopus 로고    scopus 로고
    • New channelrhodopsin with a red-shifted spectrum and rapid kinetics from Mesostigma viride
    • Govorunova, E. G., Spudich, E. N., Lane, C. E., Sineshchekov, O. A., and Spudich, J. L. (2011) New channelrhodopsin with a red-shifted spectrum and rapid kinetics from Mesostigma viride. mBio. 2, e00115-00111
    • (2011) MBio. , vol.2
    • Govorunova, E.G.1    Spudich, E.N.2    Lane, C.E.3    Sineshchekov, O.A.4    Spudich, J.L.5
  • 29
    • 33845302595 scopus 로고    scopus 로고
    • Experimental reconstruction of functional gene transfer from the tobacco plastid geneome to the nucleus
    • DOI 10.1105/tpc.106.046466
    • Stegemann, S., and Bock, R. (2006) Experimental reconstruction of functional gene transfer from the tobacco plastid genome to the nucleus. Plant Cell 18, 2869-2878 (Pubitemid 46013262)
    • (2006) Plant Cell , vol.18 , Issue.11 , pp. 2869-2878
    • Stegemann, S.1    Bock, R.2
  • 33
    • 80052461748 scopus 로고    scopus 로고
    • Rectification of the channelrhodopsin early conductance
    • Gradmann, D., Berndt, A., Schneider, F., and Hegemann, P. (2011) Rectification of the channelrhodopsin early conductance. Biophys. J. 101, 1057-1068
    • (2011) Biophys. J. , vol.101 , pp. 1057-1068
    • Gradmann, D.1    Berndt, A.2    Schneider, F.3    Hegemann, P.4
  • 34
    • 58049216319 scopus 로고    scopus 로고
    • Monitoring light-induced structural changes of Channelrhodopsin-2 by UV-visible and Fourier transform infrared spectroscopy
    • Ritter, E., Stehfest, K., Berndt, A., Hegemann, P., and Bartl, F. J. (2008) Monitoring light-induced structural changes of Channelrhodopsin-2 by UV-visible and Fourier transform infrared spectroscopy. J. Biol. Chem. 283, 35033-35041
    • (2008) J. Biol. Chem. , vol.283 , pp. 35033-35041
    • Ritter, E.1    Stehfest, K.2    Berndt, A.3    Hegemann, P.4    Bartl, F.J.5
  • 38
    • 75349085542 scopus 로고    scopus 로고
    • Structural guidance of the photocycle of channelrhodopsin-2 by an interhelical hydrogen bond
    • Bamann, C., Gueta, R., Kleinlogel, S., Nagel, G., and Bamberg, E. (2010) Structural guidance of the photocycle of channelrhodopsin-2 by an interhelical hydrogen bond. Biochemistry 49, 267-278
    • (2010) Biochemistry , vol.49 , pp. 267-278
    • Bamann, C.1    Gueta, R.2    Kleinlogel, S.3    Nagel, G.4    Bamberg, E.5
  • 42
    • 0242362271 scopus 로고    scopus 로고
    • Water Molecules in the Schiff Base Region of Bacteriorhodopsin
    • DOI 10.1021/ja037343s
    • Shibata, M., Tanimoto, T., and Kandori, H. (2003) Water molecules in the Schiff base region of bacteriorhodopsin. J. Am. Chem. Soc. 125, 13312-13313 (Pubitemid 37352090)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.44 , pp. 13312-13313
    • Shibata, M.1    Tanimoto, T.2    Kandori, H.3
  • 43
    • 60849092562 scopus 로고    scopus 로고
    • Glu 87 of channelrhodopsin-1 causes pH-dependent color tuning and fast photocurrent inactivation
    • Tsunoda, S. P., and Hegemann, P. (2009) Glu 87 of channelrhodopsin-1 causes pH-dependent color tuning and fast photocurrent inactivation. Photochem. Photobiol. 85, 564-569
    • (2009) Photochem. Photobiol. , vol.85 , pp. 564-569
    • Tsunoda, S.P.1    Hegemann, P.2
  • 45
    • 53049106598 scopus 로고    scopus 로고
    • Effect of polarization on the opsin shift in rhodopsins. 1. A combined QM/QM/MM model for bacteriorhodopsin and pharaonis sensory rhodopsin II
    • Wanko, M., Hoffmann, M., Frauenheim, T., and Elstner, M. (2008) Effect of polarization on the opsin shift in rhodopsins. 1. A combined QM/QM/MM model for bacteriorhodopsin and pharaonis sensory rhodopsin II. J. Phys. Chem. B 112, 11462-11467
    • (2008) J. Phys. Chem. B , vol.112 , pp. 11462-11467
    • Wanko, M.1    Hoffmann, M.2    Frauenheim, T.3    Elstner, M.4
  • 46
    • 53049096961 scopus 로고    scopus 로고
    • Effect of polarization on the opsin shift in rhodopsins. 2. Empirical polarization models for proteins
    • Wanko, M., Hoffmann, M., Frähmcke, J., Frauenheim, T., and Elstner, M. (2008) Effect of polarization on the opsin shift in rhodopsins. 2. Empirical polarization models for proteins. J. Phys. Chem. B 112, 11468-11478
    • (2008) J. Phys. Chem. B , vol.112 , pp. 11468-11478
    • Wanko, M.1    Hoffmann, M.2    Frähmcke, J.3    Frauenheim, T.4    Elstner, M.5
  • 48
    • 36549094506 scopus 로고
    • 2-Photon double resonance spectroscopy of bacteriorhodopsin. Assignment of the electronic and dipolar properties of the low-lying 1AG-star(-)-like and 1B-U-star+-like pi,pistar states
    • Birge, R. R., and Zhang, C. F. (1990) 2-Photon double resonance spectroscopy of bacteriorhodopsin. Assignment of the electronic and dipolar properties of the low-lying 1AG-star(-)-like and 1B-U-star+-like pi,pistar states. J. Chem. Phys. 92, 7179-7195
    • (1990) J. Chem. Phys. , vol.92 , pp. 7179-7195
    • Birge, R.R.1    Zhang, C.F.2
  • 49
    • 0031820941 scopus 로고    scopus 로고
    • The photophobic receptor from Natronobacterium pharaonis: Temperature and pH dependencies of the photocycle of sensory rhodopsin II
    • Chizhov, I., Schmies, G., Seidel, R., Sydor, J. R., Lüttenberg, B., and Engelhard, M. (1998) The photophobic receptor from Natronobacterium pharaonis. Temperature and pH dependencies of the photocycle of sensory rhodopsin II. Biophys. J. 75, 999-1009 (Pubitemid 28357540)
    • (1998) Biophysical Journal , vol.75 , Issue.2 , pp. 999-1009
    • Chizhov, I.1    Schmies, G.2    Seidel, R.3    Sydor, J.R.4    Luttenberg, B.5    Engelhard, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.